HEADER SUGAR BINDING PROTEIN 25-JUN-03 1PUM
TITLE MISTLETOE LECTIN I IN COMPLEX WITH GALACTOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LECTIN I A CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: LECTIN I B CHAIN;
COMPND 6 CHAIN: B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VISCUM ALBUM;
SOURCE 3 ORGANISM_COMMON: EUROPEAN MISTLETOE;
SOURCE 4 ORGANISM_TAXID: 3972;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: VISCUM ALBUM;
SOURCE 7 ORGANISM_COMMON: EUROPEAN MISTLETOE;
SOURCE 8 ORGANISM_TAXID: 3972
KEYWDS PROTEIN-SUGAR COMPLEX, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.KRAUSPENHAAR,W.VOELTER,S.STOEVA,A.MIKHAILOV,N.KONAREVA,C.BETZEL
REVDAT 6 29-JUL-20 1PUM 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 13-JUL-11 1PUM 1 VERSN
REVDAT 4 24-FEB-09 1PUM 1 VERSN
REVDAT 3 14-MAR-06 1PUM 1 JRNL
REVDAT 2 03-MAY-05 1PUM 1 JRNL
REVDAT 1 25-JUN-04 1PUM 0
JRNL AUTH R.MIKESKA,R.WACKER,R.ARNI,T.P.SINGH,A.MIKHAILOV,
JRNL AUTH 2 A.GABDOULKHAKOV,W.VOELTER,C.BETZEL
JRNL TITL MISTLETOE LECTIN I IN COMPLEX WITH GALACTOSE AND LACTOSE
JRNL TITL 2 REVEALS DISTINCT SUGAR-BINDING PROPERTIES
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 61 17 2005
JRNL REFN ESSN 1744-3091
JRNL PMID 16508080
JRNL DOI 10.1107/S1744309104031501
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 45303
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2388
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3506
REMARK 3 BIN FREE R VALUE : 0.3797
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 201
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3918
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 226
REMARK 3 SOLVENT ATOMS : 361
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.30
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.569
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.05
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.870
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.008 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 2.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9073
REMARK 200 MONOCHROMATOR : GERMANIUM 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46562
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 25.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.42300
REMARK 200 R SYM FOR SHELL (I) : 0.39300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.580
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, GLYCIN-HCL,
REMARK 280 GALACTOSE, DIOXAN, PH 2.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 207.30067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 103.65033
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 155.47550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 51.82517
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 259.12583
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 207.30067
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 103.65033
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 51.82517
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 155.47550
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 259.12583
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER WHICH ARE ARRANGED ALONG
REMARK 300 A SIX-FOLD-AXIS.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B 208 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 43 21.58 -69.61
REMARK 500 ASN A 74 -1.62 -151.85
REMARK 500 ASP A 126 3.10 -65.70
REMARK 500 ILE A 163 -73.61 -117.39
REMARK 500 LEU A 222 -153.90 -120.37
REMARK 500 SER A 223 -81.53 -80.97
REMARK 500 PRO A 224 80.86 -62.81
REMARK 500 CYS B 5 47.11 -149.45
REMARK 500 ARG B 17 123.54 -32.95
REMARK 500 ASN B 18 18.66 59.78
REMARK 500 VAL B 199 -14.62 -47.66
REMARK 500 ALA B 237 126.96 -39.73
REMARK 500 GLN B 238 28.33 48.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PUU RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH LACTOSE
DBREF 1PUM A 1 249 UNP P81446 ML1_VISAL 34 282
DBREF 1PUM B 1 263 UNP P81446 ML1_VISAL 302 564
SEQRES 1 A 249 TYR GLU ARG LEU SER LEU ARG THR VAL GLN GLN THR THR
SEQRES 2 A 249 GLY ALA GLU TYR PHE SER PHE ILE THR LEU LEU ARG ASP
SEQRES 3 A 249 PHE VAL SER SER GLY SER PHE SER ASN GLN ILE PRO LEU
SEQRES 4 A 249 LEU ARG GLN SER THR ILE PRO VAL SER GLU GLY GLN ARG
SEQRES 5 A 249 PHE VAL LEU VAL GLU LEU THR ASN ALA GLY GLY ASP SER
SEQRES 6 A 249 ILE THR ALA ALA ILE ASP VAL THR ASN LEU TYR VAL VAL
SEQRES 7 A 249 ALA TYR ARG ALA GLY ASP GLN SER TYR PHE LEU LYS ASP
SEQRES 8 A 249 ALA PRO ALA GLY ALA GLU THR GLN ASP PHE ALA GLY THR
SEQRES 9 A 249 THR ARG SER SER LEU PRO PHE ASN GLY SER TYR PRO ASP
SEQRES 10 A 249 LEU GLU ARG TYR ALA GLY HIS ARG ASP GLN ILE PRO LEU
SEQRES 11 A 249 GLY ILE ASP GLN LEU ILE ALA SER VAL THR ALA LEU ARG
SEQRES 12 A 249 PHE PRO GLY GLY SER THR ARG THR GLN ALA ARG SER ILE
SEQRES 13 A 249 LEU ILE LEU ILE GLN MET ILE SER GLU ALA ALA ARG PHE
SEQRES 14 A 249 ASN PRO ILE LEU TRP ARG ALA ARG GLN TYR ILE ASN SER
SEQRES 15 A 249 GLY ALA SER PHE LEU PRO ASP VAL TYR MET LEU GLU LEU
SEQRES 16 A 249 GLU THR SER TRP GLY GLN GLN SER THR GLN VAL GLN HIS
SEQRES 17 A 249 SER THR ASP GLY VAL PHE ASN ASN PRO ILE ALA LEU ALA
SEQRES 18 A 249 LEU SER PRO GLY SER VAL VAL THR LEU THR ASN VAL ARG
SEQRES 19 A 249 ASP VAL ILE ALA SER LEU ALA ILE MET LEU PHE VAL CYS
SEQRES 20 A 249 GLY GLU
SEQRES 1 B 263 ASP ASP VAL THR CYS SER ALA SER GLU PRO ILE VAL ARG
SEQRES 2 B 263 ILE VAL GLY ARG ASN GLY MET THR VAL ASP VAL ARG ASP
SEQRES 3 B 263 ASP ASP PHE GLN ASP GLY ASN GLN ILE GLN LEU TRP PRO
SEQRES 4 B 263 SER LYS SER ASN ASN ASP PRO ASN GLN LEU TRP THR ILE
SEQRES 5 B 263 LYS LYS ASP GLY THR ILE ARG SER ASN GLY SER CYS LEU
SEQRES 6 B 263 THR THR TYR GLY TYR THR ALA GLY VAL TYR VAL MET ILE
SEQRES 7 B 263 PHE ASP CYS ASN THR ALA VAL ARG GLU ALA THR ILE TRP
SEQRES 8 B 263 GLN ILE TRP GLY ASN GLY THR ILE ILE ASN PRO ARG SER
SEQRES 9 B 263 ASN LEU VAL LEU ALA ALA SER SER GLY ILE LYS GLY THR
SEQRES 10 B 263 THR LEU THR VAL GLN THR LEU ASP TYR THR LEU GLY GLN
SEQRES 11 B 263 GLY TRP LEU ALA GLY ASN ASP THR ALA PRO ARG GLU VAL
SEQRES 12 B 263 THR ILE TYR GLY PHE ARG ASP LEU CYS MET GLU SER ALA
SEQRES 13 B 263 GLY GLY SER VAL TRP VAL GLU THR CYS THR ALA GLY GLN
SEQRES 14 B 263 GLU ASN GLN ARG TRP ALA LEU TYR GLY ASP GLY SER ILE
SEQRES 15 B 263 ARG PRO LYS GLN ASN GLN SER GLN CYS LEU THR ASN GLY
SEQRES 16 B 263 ARG ASP SER VAL SER THR VAL ILE ASN ILE VAL SER CYS
SEQRES 17 B 263 SER ALA GLY SER SER GLY GLN ARG TRP VAL PHE THR ASN
SEQRES 18 B 263 ALA GLY ALA ILE LEU ASN LEU LYS ASN GLY LEU ALA MET
SEQRES 19 B 263 ASP VAL ALA GLN ALA ASN PRO ALA LEU ALA ARG ILE ILE
SEQRES 20 B 263 ILE TYR PRO ALA THR GLY ASN PRO ASN GLN MET TRP LEU
SEQRES 21 B 263 PRO VAL PRO
MODRES 1PUM ASN A 112 ASN GLYCOSYLATION SITE
MODRES 1PUM ASN B 61 ASN GLYCOSYLATION SITE
MODRES 1PUM ASN B 96 ASN GLYCOSYLATION SITE
MODRES 1PUM ASN B 136 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NDG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET FUL E 2 10
HET NAG A1004 14
HET CL A1026 1
HET CL A1027 1
HET SO4 A1028 5
HET SO4 A1029 5
HET GOL A1010 6
HET GOL A1011 6
HET GOL A1012 6
HET GOL A1014 6
HET GOL A1017 6
HET GOL A1024 6
HET GOL A1025 6
HET GAL B1008 12
HET GAL B1009 12
HET GOL B1013 6
HET GOL B1015 6
HET GOL B1016 6
HET GOL B1018 6
HET GOL B1019 6
HET GOL B1020 6
HET GOL B1021 6
HET GOL B1022 6
HET GOL B1023 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE
HETNAM FUL BETA-L-FUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 5(C8 H15 N O6)
FORMUL 3 NDG C8 H15 N O6
FORMUL 5 FUL C6 H12 O5
FORMUL 7 CL 2(CL 1-)
FORMUL 9 SO4 2(O4 S 2-)
FORMUL 11 GOL 16(C3 H8 O3)
FORMUL 18 GAL 2(C6 H12 O6)
FORMUL 29 HOH *361(H2 O)
HELIX 1 1 THR A 13 VAL A 28 1 16
HELIX 2 2 GLY A 95 GLN A 99 5 5
HELIX 3 3 SER A 114 GLY A 123 1 10
HELIX 4 4 HIS A 124 ILE A 128 5 5
HELIX 5 5 GLY A 131 PHE A 144 1 14
HELIX 6 6 SER A 148 ILE A 163 1 16
HELIX 7 7 ILE A 163 PHE A 169 1 7
HELIX 8 8 PHE A 169 GLY A 183 1 15
HELIX 9 9 ASP A 189 SER A 209 1 21
HELIX 10 10 VAL A 233 ILE A 237 1 5
HELIX 11 11 GLY B 16 MET B 20 5 5
HELIX 12 12 ASP B 26 ASP B 28 5 3
HELIX 13 13 ASP B 45 LEU B 49 5 5
HELIX 14 14 VAL B 85 ILE B 90 5 6
HELIX 15 15 THR B 127 GLY B 131 5 5
HELIX 16 16 GLY B 147 LEU B 151 5 5
HELIX 17 17 GLN B 169 ASN B 171 5 3
HELIX 18 18 SER B 212 GLN B 215 5 4
HELIX 19 19 GLN B 238 ALA B 244 5 7
HELIX 20 20 ASN B 254 MET B 258 5 5
SHEET 1 A 6 GLU A 2 THR A 8 0
SHEET 2 A 6 PHE A 53 ASN A 60 1 O THR A 59 N THR A 8
SHEET 3 A 6 SER A 65 ASP A 71 -1 O ALA A 68 N VAL A 56
SHEET 4 A 6 VAL A 77 ALA A 82 -1 O ALA A 79 N ALA A 69
SHEET 5 A 6 GLN A 85 PHE A 88 -1 O TYR A 87 N TYR A 80
SHEET 6 A 6 THR A 105 SER A 108 1 O SER A 107 N PHE A 88
SHEET 1 B 2 SER A 29 SER A 34 0
SHEET 2 B 2 ILE A 37 LEU A 40 -1 O ILE A 37 N SER A 34
SHEET 1 C 2 VAL A 213 ALA A 221 0
SHEET 2 C 2 VAL A 227 ASN A 232 -1 O LEU A 230 N ILE A 218
SHEET 1 D 5 ILE B 11 VAL B 12 0
SHEET 2 D 5 TRP B 50 ILE B 52 -1 O TRP B 50 N VAL B 12
SHEET 3 D 5 ILE B 58 SER B 60 -1 O ARG B 59 N THR B 51
SHEET 4 D 5 SER B 63 THR B 67 -1 O SER B 63 N SER B 60
SHEET 5 D 5 VAL B 76 PHE B 79 -1 O MET B 77 N THR B 66
SHEET 1 E 2 ILE B 14 VAL B 15 0
SHEET 2 E 2 LEU B 133 ALA B 134 -1 O LEU B 133 N VAL B 15
SHEET 1 F 2 THR B 21 VAL B 24 0
SHEET 2 F 2 ILE B 35 TRP B 38 -1 O TRP B 38 N THR B 21
SHEET 1 G 4 GLN B 92 ILE B 93 0
SHEET 2 G 4 ILE B 99 ASN B 101 -1 O ILE B 100 N GLN B 92
SHEET 3 G 4 LEU B 106 ALA B 109 -1 O LEU B 106 N ASN B 101
SHEET 4 G 4 THR B 120 GLN B 122 -1 O GLN B 122 N VAL B 107
SHEET 1 H 4 ILE B 182 PRO B 184 0
SHEET 2 H 4 ARG B 173 LEU B 176 -1 N ALA B 175 O ARG B 183
SHEET 3 H 4 ARG B 141 TYR B 146 -1 N VAL B 143 O TRP B 174
SHEET 4 H 4 LEU B 260 VAL B 262 -1 O LEU B 260 N TYR B 146
SHEET 1 I 2 CYS B 152 ALA B 156 0
SHEET 2 I 2 SER B 159 GLU B 163 -1 O SER B 159 N ALA B 156
SHEET 1 J 2 GLN B 190 THR B 193 0
SHEET 2 J 2 ASN B 204 SER B 207 -1 O VAL B 206 N CYS B 191
SHEET 1 K 2 TRP B 217 PHE B 219 0
SHEET 2 K 2 ILE B 225 ASN B 227 -1 O LEU B 226 N VAL B 218
SHEET 1 L 2 ALA B 233 VAL B 236 0
SHEET 2 L 2 ILE B 246 TYR B 249 -1 O ILE B 247 N ASP B 235
SSBOND 1 CYS A 247 CYS B 5 1555 1555 2.03
SSBOND 2 CYS B 64 CYS B 81 1555 1555 2.04
SSBOND 3 CYS B 152 CYS B 165 1555 1555 2.03
SSBOND 4 CYS B 191 CYS B 208 1555 1555 2.04
LINK ND2 ASN A 112 C1 NAG A1004 1555 1555 1.45
LINK ND2 ASN B 61 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN B 96 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN B 136 C1 NAG C 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NDG C 2 1555 1555 1.39
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.38
LINK O3 NAG E 1 C1 FUL E 2 1555 1555 1.40
CRYST1 106.826 106.826 310.951 90.00 90.00 120.00 P 65 2 2 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009360 0.005400 0.000000 0.00000
SCALE2 0.000000 0.010810 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003220 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
